SitesHMM for PF01817 (CM

5gmuB Crystal structure of chorismate mutase like domain of bifunctional dahp synthase of bacillus subtilis in complex with chlorogenic acid (see paper)
68.0 bits, 100% coverage: 1:79/79 of HMM aligns to 9:86/87 of 5gmuB

HMM
sites
5gmuB

R

R

K

Q

E

K

I

A

D

D

E

E

I

L

D

N

R

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E

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L

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E

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R

M

G

E

N

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V

A

V

K

K

E

E

I

I

A

G

E

K

Y

A

K

K

K

E

E

A

N

Q

G

G

L

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P

N

V
x
R

L
x
F

D
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D

P

P

E

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R

E
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E

E

R

E

T

V

M

L

L

E

N

R

N

L

I

R

I

E

E

-

N

-

D

G

G

A

P

E

-

L

-

G

-

L

F

D

E

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N

E

S

A

T

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Q

K

H

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I

F

F

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K

E

E

I

I

I
x
F

S
x
K

E

A

S

G

R
x
L

A

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L

L

Q
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Q

K

E

binding (1R,3R,4S,5R)-3-[3-[3,4-bis(oxidanyl)phenyl]propanoyloxy]-1,4,5-tris(oxidanyl)cyclohexane-1-carboxylic acid: R26 (= R18), R44 (≠ V36), F45 (≠ L37), D46 (= D38), E50 (= E42), F78 (≠ I71), K79 (≠ S72), L82 (≠ R75), Q85 (= Q78)

6al9A Crystal structure of chorismate mutase from helicobacter pylori in complex with prephenate
67.7 bits, 100% coverage: 1:79/79 of HMM aligns to 8:83/90 of 6al9A

HMM
sites
6al9A

R

R

K

A

E

E

I

I

D

D

E

A

I

L

D

D

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N

E

E

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L

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R

M

L

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E

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K

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A

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Y

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K

K

Q

E

-

N

-

G

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x
C

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E

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E

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I
x
F

S

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I

S
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S

R

R

A

K

L

F

Q
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Q

K

E

binding prephenic acid: R25 (= R18), C43 (≠ D38), R46 (= R41), E47 (= E42), F75 (≠ I71), S78 (= S74), Q82 (= Q78)

6al9B Crystal structure of chorismate mutase from helicobacter pylori in complex with prephenate
67.7 bits, 100% coverage: 1:79/79 of HMM aligns to 9:84/91 of 6al9B

HMM
sites
6al9B

R

R

K

A

E

E

I

I

D

D

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A

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D

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N

E

E

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I

A

A

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L

Y

I

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K

K

Q

E

-

N

-

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C

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E

I

S

S

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R

A

K

L

F

Q
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Q

K

E

binding pyruvic acid: I33 (= I25), Q83 (= Q78)

5j6fA Crystal structure of dah7ps-cm complex from geobacillus sp. With prephenate (see paper)
66.0 bits, 100% coverage: 1:79/79 of HMM aligns to 8:85/352 of 5j6fA

HMM
sites
5j6fA

R

R

K

A

E

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D

D

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E

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N

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R

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I

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K

K

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G

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x
Y

D
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D

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R

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x
M

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E

E

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H

-

N

-

D

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G

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L

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I

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A

S

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A

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L

L

Q

Q

K

E

binding prephenic acid: R25 (= R18), I32 (= I25), K36 (= K29), Y44 (≠ L37), D45 (= D38), R48 (= R41), M52 (≠ V45)

Sites not aligning to the query:

binding manganese (ii) ion: 124, 294, 320, 331

P0A9J8 Bifunctional chorismate mutase/prephenate dehydratase; Chorismate mutase-prephenate dehydratase; P-protein; EC 5.4.99.5; EC 4.2.1.51 from Escherichia coli (strain K12)
65.6 bits, 100% coverage: 1:79/79 of HMM aligns to 11:89/386 of P0A9J8

HMM
sites
P0A9J8

R
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R

K

E

E

K

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D

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R

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R

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E

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L

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K

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E

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Q

K

Q

R11 (= R1) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
R28 (= R18) mutation R->A,K: Important decrease in catalytic efficiency and affinity.
K39 (= K29) mutation K->A,Q,R: Important decrease in catalytic efficiency and affinity.
E52 (= E42) mutation E->A,D,Q: Important decrease in catalytic efficiency and affinity.
Q88 (= Q78) mutation Q->A,E,K: Important decrease in catalytic efficiency and affinity.

2h9dD Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
65.4 bits, 99% coverage: 1:78/79 of HMM aligns to 14:90/100 of 2h9dD

HMM
sites
2h9dD

R

R

K
x
E

E

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D

E

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I

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Q

L

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K

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F

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K

K

A

E

-

N

S

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A

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M

L

L

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A

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N

G

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E

Q
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Q

binding calcium ion: E15 (≠ K2), D18 (= D5)
binding pyruvic acid: R31 (= R18), K42 (= K29), M57 (≠ V45), Q90 (= Q78)

Q51507 Isochorismate pyruvate lyase; IPL; Chorismate mutase; CM; Salicylate biosynthesis protein; EC 4.2.99.21; EC 5.4.99.5 from Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) (see 5 papers)
65.4 bits, 99% coverage: 1:78/79 of HMM aligns to 14:90/101 of Q51507

HMM
sites
Q51507

R
|
R

K

E

E

A

I

I

D

D

E

R

I

I

D

D

R

L

E

D

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M

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K

E
x
A

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F

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K

K
x
A

E

-

N

S

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A

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E

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N

G

G

L

L

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D

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A

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E

K

G

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F

F

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E

Q

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H

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Y

R
x
I

A

A

L

E

Q
|
Q

R14 (= R1) binding substrate
R31 (= R18) binding substrate
A37 (≠ E24) mutation to I: Increases the rate constant for the mutase activity by a factor of 1000, and also increases the lyase catalytic efficiency by a factor of 6.
K42 (= K29) binding substrate; mutation to A: Active across the entire pH range from 4 to 9. 11-fold reduction of the affinity for isochorismate and 7-fold reduction of the catalytic efficiency for lyase activity. 6-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity.; mutation to E: Loss of both lyase and mutase activity at any pH tested.; mutation to H: At pH 5, 15-fold reduction of the affinity for isochorismate, but only a slight reduction of the catalytic efficiency for lyase activity. At pH 7.5, 13-fold reduction of the affinity for isochorismate and 4-fold reduction of the catalytic efficiency for lyase activity. At pH 5, strong reduction of the affinity for chorismate, but only a 2-fold reduction of the catalytic efficiency for mutase activity. At pH 7.5, strong reduction of the affinity for chorismate, but only a slight reduction of the catalytic efficiency for mutase activity.; mutation to Q: Loss of mutase activity. 15-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity.
A43 (≠ K30) mutation to P: Slight reduction of the affinity for isochorismate and of the catalytic efficiency for isochorismate-pyruvate lyase activity. Slight reduction of the affinity for chorismate and of the catalytic efficiency for mutase activity.
I87 (≠ R75) mutation to T: 4-fold reduction of the affinity for isochorismate and 3-fold reduction of the catalytic efficiency for isochorismate-pyruvate lyase activity. 4-fold reduction of the affinity for chorismate and 15-fold reduction of the catalytic efficiency for mutase activity.
Q90 (= Q78) binding substrate

P39912 Protein AroA(G); EC 2.5.1.54; EC 5.4.99.5 from Bacillus subtilis (strain 168) (see paper)
63.1 bits, 100% coverage: 1:79/79 of HMM aligns to 10:87/358 of P39912

HMM
sites
P39912

R

R

K

Q

E

K

I

A

D

D

E

E

I

L

D

N

R

L

E

Q

L

I

L

L

E

K

L

L

L

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A

N

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G

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N

L

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A

V

K

K

E

E

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I

A

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K

Y

A

K

K

K

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G

G

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P

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N

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N

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E

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N

-

D

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G

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I

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F

S

K

E

A

S

G

R

L

A

E

L

L

Q

Q

K

E

Sites not aligning to the query:

2 modified: Phosphoserine

2gtvX Nmr structure of monomeric chorismate mutase from methanococcus jannaschii (see paper)
60.5 bits, 100% coverage: 1:79/79 of HMM aligns to 9:95/104 of 2gtvX

HMM
sites
2gtvX

R
|
R

K

K

E

K

I

I

D

D

E

E

I

I

D

D

R

N

E

K

L

I

L

L

E

K

-

A

-

R

-

W

-

P

-

W

-

A

-

E

-

K

L

L

L

I

A

A

E

E

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R

M

N

E

S

L

L

A

A

K

K

E

D

I
x
V

A

A

E

E

Y

I

K
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K

K

N

E

Q

N

L

G

G

L

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P

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D
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D

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E

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R

E
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E

E

K

E

Y

V

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L

Y

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D

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G

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A

C

E

K

E

E

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H

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N

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E

E

N

A

I

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G

E

I

K

K

I

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F

F

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E

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I

I

S

E

E

H

S
x
N

R

K

A

A

L

L

Q
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Q

K

K

binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R9 (= R1), R34 (= R18), V41 (≠ I25), K45 (= K29), D54 (= D38), R57 (= R41), E58 (= E42), N90 (≠ S74), Q94 (= Q78)

3nvtA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e (see paper)
53.4 bits, 100% coverage: 1:79/79 of HMM aligns to 3:75/345 of 3nvtA

HMM
sites
3nvtA

R

R

K

T

E

Q

I

V

D

D

E

Q

I

L

D

N

R

I

E

D

L

L

E

E

L

L

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A

E

N

L

L

A

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K

Q

E

E

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A

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K

Y

I

K

K

K

-

E

-

N

-

G

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L

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D

D

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P

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E

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E

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A

A

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E

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A

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K

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I

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F

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K

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A

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G

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A

E

L

L

Q

Q

K

E

Sites not aligning to the query:

binding manganese (ii) ion: 114, 284, 310, 321

3tfcA 1.95 angstrom crystal structure of a bifunctional 3-deoxy-7- phosphoheptulonate synthase/chorismate mutase (aroa) from listeria monocytogenes egd-e in complex with phosphoenolpyruvate (see paper)
52.2 bits, 100% coverage: 1:79/79 of HMM aligns to 2:74/343 of 3tfcA

HMM
sites
3tfcA

R

R

K

T

E

Q

I

V

D

D

E

Q

I

L

D

N

R

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E

D

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L

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E

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K

Y

I

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K

K

L

E

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N

-

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D

D

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P

E

L

R

R

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E

E

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E

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M

L

L

E

N

R

T

L

I

R

L

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A

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-

A

A

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E

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D

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K

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F

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K

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E

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F

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K

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A

E

L

L

Q

Q

K

E

Sites not aligning to the query:

binding manganese (ii) ion: 113, 283, 309, 320
binding phosphoenolpyruvate: 137, 193, 196, 218, 248, 283

2fp2B Secreted chorismate mutase from mycobacterium tuberculosis (see paper)
48.0 bits, 87% coverage: 10:78/79 of HMM aligns to 5:73/163 of 2fp2B

HMM
sites
2fp2B

E

E

L

L

L

V

E

D

L

A

A

A

E

E

R
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R

M

L

E

E

L

V

A

A

K

D

E

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A

A

E

A

Y

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K

K

W

E

R

N

A

G

Q

L

L

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P

V
x
I

L
x
E

D
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D

P

S

E

G

R
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R

E

V

E

E

E

Q

V
x
Q

L

L

E

A

R

K

L

L

R

G

E

E

G

D

A

A

E

R

E

S

L

Q

G

H

L

I

D

D

P

P

E

D

A

Y

V

V

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T

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R

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F

F

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D

E

D

I

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I

S

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A

S
x
T

R
x
E

A

A

L

I

Q
x
E

active site: R13 (= R18), K24 (= K29), D33 (= D38), T69 (≠ S74), E70 (≠ R75), E73 (≠ Q78)
binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R13 (= R18), K24 (= K29), I31 (≠ V36), E32 (≠ L37), D33 (= D38), R36 (= R41), Q40 (≠ V45), I66 (= I71), T69 (≠ S74), E70 (≠ R75), E73 (≠ Q78)

Sites not aligning to the query:

active site: 98
binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: 98

2ao2A The 2.07 angstrom crystal structure of mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions (see paper)
48.0 bits, 87% coverage: 10:78/79 of HMM aligns to 7:75/165 of 2ao2A

HMM
sites
2ao2A

E

E

L

L

L

V

E

D

L

A

A

A

E

E

R
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R

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L

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E

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A

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x
T

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x
E

active site: R15 (= R18), K26 (= K29), D35 (= D38), T71 (≠ S74), E72 (≠ R75), E75 (≠ Q78)
binding sulfate ion: K26 (= K29), R38 (= R41)

Sites not aligning to the query:

active site: 100
binding sulfate ion: 100

2ao2B The 2.07 angstrom crystal structure of mycobacterium tuberculosis chorismate mutase reveals unexpected gene duplication and suggests a role in host-pathogen interactions (see paper)
48.0 bits, 87% coverage: 10:78/79 of HMM aligns to 7:75/165 of 2ao2B

HMM
sites
2ao2B

E

E

L

L

L

V

E

D

L

A

A

A

E

E

R
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R

M

L

E

E

L

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K

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L

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P

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I

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x
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D

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R

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E

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x
Q

L

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D

A

A

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A

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x
E

active site: R15 (= R18), K26 (= K29), D35 (= D38), T71 (≠ S74), E72 (≠ R75), E75 (≠ Q78)
binding sulfate ion: K26 (= K29), R38 (= R41), Q42 (≠ V45)
binding tryptophan: L31 (= L34), P32 (= P35), I33 (≠ V36), E34 (≠ L37)

Sites not aligning to the query:

active site: 100

2h9cA Native crystal structure of the isochorismate-pyruvate lyase from pseudomonas aeruginosa (see paper)
45.8 bits, 99% coverage: 1:78/79 of HMM aligns to 14:82/88 of 2h9cA

HMM
sites
2h9cA

R

R

K

E

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x
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-

E

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N

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Y

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Q

binding nitrate ion: Q26 (≠ E13), R30 (≠ E17), R31 (= R18), K36 (= K23), A37 (≠ E24), R40 (≠ E27), R45 (= R41), M49 (≠ V45), I75 (= I71), Y78 (≠ S74)

P9WIB9 Secreted chorismate mutase; CM; *MtCM; EC 5.4.99.5 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 4 papers)
47.4 bits, 87% coverage: 10:78/79 of HMM aligns to 41:109/199 of P9WIB9

HMM
sites
P9WIB9

E

E

L

L

L

V

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L

A

A

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L

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R49 (= R18) mutation to A: Less than 1% of the wild-type enzyme activity.
K60 (= K29) mutation to A: Less than 1% of the wild-type enzyme activity.
D69 (= D38) mutation to A: No effect on the enzyme activity.
R72 (= R41) mutation to A: Less than 1% of the wild-type enzyme activity.
T105 (≠ S74) mutation to A: 20% of the wild-type enzyme activity.
E109 (≠ Q78) mutation to A: 10% of the wild-type enzyme activity.; mutation to Q: 40% of the wild-type enzyme activity at pH 7.5 and 27% of the wild-type enzyme activity at pH 4.

Sites not aligning to the query:

1:33 signal peptide
134 R→A: Less than 1% of the wild-type enzyme activity.
160 modified: Disulfide link with 193
193 modified: Disulfide link with 160

Q7CHH5 Secreted chorismate mutase; CM; *YpCM; EC 5.4.99.5 from Yersinia pestis (see paper)
43.8 bits, 84% coverage: 14:79/79 of HMM aligns to 39:104/186 of Q7CHH5

HMM
sites
Q7CHH5

L

L

L

I

A

N

E

E

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Y

Sites not aligning to the query:

33 modified: Disulfide link with 148
148 modified: Disulfide link with 33

5ckxD Non-covalent complex of dahp synthase and chorismate mutase from mycobacterium tuberculosis with bound transition state analog and feedback effectors tyrosine and phenylalanine (see paper)
45.1 bits, 68% coverage: 1:54/79 of HMM aligns to 7:61/79 of 5ckxD

HMM
sites
5ckxD

R

R

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E

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I

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E

D

binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: R24 (= R18), S28 (≠ A22), I31 (= I25), R35 (≠ K29), R47 (= R41), E48 (= E42)

Sites not aligning to the query:

binding 8-hydroxy-2-oxa-bicyclo[3.3.1]non-6-ene-3,5-dicarboxylic acid: 70

2h9dA Pyruvate-bound structure of the isochorismate-pyruvate lyase from pseudomonas aerugionsa (see paper)
39.6 bits, 99% coverage: 1:78/79 of HMM aligns to 14:80/84 of 2h9dA

HMM
sites
2h9dA

R

R

K

E

E

A

I

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M

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A

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Q

binding pyruvic acid: R31 (= R18), M47 (≠ V45)

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory